GENTAUR Molecular Products.

 TGFB3_RAT               Reviewed;         412 AA.
 Q07258; Q56A31;
 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
 01-FEB-1996, sequence version 2.
 10-OCT-2018, entry version 143.
 RecName: Full=Transforming growth factor beta-3 proprotein;
 Contains:
   RecName: Full=Latency-associated peptide;
            Short=LAP;
 Contains:
   RecName: Full=Transforming growth factor beta-3;
            Short=TGF-beta-3;
 Flags: Precursor;
 Name=Tgfb3; Synonyms=Tgf-b3;
 Rattus norvegicus (Rat).
 Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
 Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
 Muroidea; Muridae; Murinae; Rattus.
 NCBI_TaxID=10116;
 [1]
 NUCLEOTIDE SEQUENCE [MRNA].
 STRAIN=Wistar; TISSUE=Lung;
 PubMed=7852342; DOI=10.1074/jbc.270.6.2722;
 Wang J., Kuliszewski M., Yee W., Sedlackova L., Xu J., Tseu I.,
 Post M.;
 "Cloning and expression of glucocorticoid-induced genes in fetal rat
 lung fibroblasts. Transforming growth factor-beta 3.";
 J. Biol. Chem. 270:2722-2728(1995).
 [2]
 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
 TISSUE=Brain;
 PubMed=15489334; DOI=10.1101/gr.2596504;
 The MGC Project Team;
 "The status, quality, and expansion of the NIH full-length cDNA
 project: the Mammalian Gene Collection (MGC).";
 Genome Res. 14:2121-2127(2004).
 [3]
 NUCLEOTIDE SEQUENCE [MRNA] OF 159-213.
 PubMed=8509457; DOI=10.1083/jcb.121.6.1397;
 McKinnon R.D., Piras G., Ida J., Dubois-Dalq M.;
 "A role for TGF-beta in oligodendrocyte differentiation.";
 J. Cell Biol. 121:1397-1407(1993).
 -!- FUNCTION: Transforming growth factor beta-3 proprotein: Precursor
     of the Latency-associated peptide (LAP) and Transforming growth
     factor beta-3 (TGF-beta-3) chains, which constitute the regulatory
     and active subunit of TGF-beta-3, respectively.
     {ECO:0000250|UniProtKB:P01137, ECO:0000250|UniProtKB:P04202}.
 -!- FUNCTION: Latency-associated peptide: Required to maintain the
     Transforming growth factor beta-3 (TGF-beta-3) chain in a latent
     state during storage in extracellular matrix (By similarity).
     Associates non-covalently with TGF-beta-3 and regulates its
     activation via interaction with 'milieu molecules', such as LTBP1
     and LRRC32/GARP, that control activation of TGF-beta-3 (By
     similarity). Interaction with integrins results in distortion of
     the Latency-associated peptide chain and subsequent release of the
     active TGF-beta-3 (By similarity). {ECO:0000250|UniProtKB:P01137,
     ECO:0000250|UniProtKB:P04202, ECO:0000250|UniProtKB:P17125}.
 -!- FUNCTION: Transforming growth factor beta-3: Multifunctional
     protein that regulates embryogenesis and cell differentiation and
     is required in various processes such as secondary palate
     development (By similarity). Activation into mature form follows
     different steps: following cleavage of the proprotein in the Golgi
     apparatus, Latency-associated peptide (LAP) and Transforming
     growth factor beta-3 (TGF-beta-3) chains remain non-covalently
     linked rendering TGF-beta-3 inactive during storage in
     extracellular matrix (By similarity). At the same time, LAP chain
     interacts with 'milieu molecules', such as LTBP1 and LRRC32/GARP
     that control activation of TGF-beta-3 and maintain it in a latent
     state during storage in extracellular milieus (By similarity).
     TGF-beta-3 is released from LAP by integrins: integrin-binding
     results in distortion of the LAP chain and subsequent release of
     the active TGF-beta-3 (By similarity). Once activated following
     release of LAP, TGF-beta-3 acts by binding to TGF-beta receptors
     (TGFBR1 and TGFBR2), which transduce signal (By similarity).
     {ECO:0000250|UniProtKB:P01137, ECO:0000250|UniProtKB:P04202,
     ECO:0000250|UniProtKB:P17125}.
 -!- SUBUNIT: Interacts with ASPN (By similarity). Latency-associated
     peptide: Homodimer; disulfide-linked. Latency-associated peptide:
     Interacts with Transforming growth factor beta-3 (TGF-beta-3)
     chain; interaction is non-covalent and maintains (TGF-beta-3) in a
     latent state (By similarity). Latency-associated peptide:
     Interacts with LRRC32/GARP; leading to regulate activation of TGF-
     beta-3 and promote epithelial fusion during palate development (By
     similarity). Latency-associated peptide: Interacts (via cell
     attachment site) with integrins, leading to release of the active
     TGF-beta-3 (By similarity). Transforming growth factor beta-3:
     Homodimer; disulfide-linked (By similarity). Transforming growth
     factor beta-3: Interacts with TGF-beta receptors (TGFBR1 and
     TGFBR2), leading to signal transduction (By similarity).
     {ECO:0000250|UniProtKB:P01137, ECO:0000250|UniProtKB:P04202,
     ECO:0000250|UniProtKB:P10600, ECO:0000250|UniProtKB:P17125}.
 -!- SUBCELLULAR LOCATION: Latency-associated peptide: Secreted,
     extracellular space, extracellular matrix
     {ECO:0000250|UniProtKB:P01137}.
 -!- SUBCELLULAR LOCATION: Transforming growth factor beta-3: Secreted
     {ECO:0000250|UniProtKB:P01137}.
 -!- PTM: Transforming growth factor beta-3 proprotein: The precursor
     proprotein is cleaved in the Golgi apparatus to form Transforming
     growth factor beta-3 (TGF-beta-3) and Latency-associated peptide
     (LAP) chains, which remain non-covalently linked, rendering TGF-
     beta-3 inactive. {ECO:0000250|UniProtKB:P01137}.
 -!- PTM: Methylated at Gln-293 by N6AMT1.
     {ECO:0000250|UniProtKB:P10600}.
 -!- SIMILARITY: Belongs to the TGF-beta family. {ECO:0000305}.
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 EMBL; U03491; AAA67915.1; -; mRNA.
 EMBL; BC092195; AAH92195.1; -; mRNA.
 EMBL; X71903; CAA50722.1; -; mRNA.
 PIR; A55706; A55706.
 RefSeq; NP_037306.1; NM_013174.2.
 UniGene; Rn.7018; -.
 ProteinModelPortal; Q07258; -.
 SMR; Q07258; -.
 STRING; 10116.ENSRNOP00000013516; -.
 PhosphoSitePlus; Q07258; -.
 PaxDb; Q07258; -.
 Ensembl; ENSRNOT00000013516; ENSRNOP00000013516; ENSRNOG00000009867.
 GeneID; 25717; -.
 KEGG; rno:25717; -.
 UCSC; RGD:3851; rat.
 CTD; 7043; -.
 RGD; 3851; Tgfb3.
 eggNOG; KOG3900; Eukaryota.
 eggNOG; ENOG410XT8Z; LUCA.
 GeneTree; ENSGT00910000143982; -.
 HOGENOM; HOG000290198; -.
 HOVERGEN; HBG074115; -.
 InParanoid; Q07258; -.
 KO; K13377; -.
 OMA; PEPSVMT; -.
 OrthoDB; EOG091G0BMM; -.
 PhylomeDB; Q07258; -.
 TreeFam; TF351793; -.
 Reactome; R-RNO-114608; Platelet degranulation.
 Reactome; R-RNO-2129379; Molecules associated with elastic fibres.
 PRO; PR:Q07258; -.
 Proteomes; UP000002494; Chromosome 6.
 Bgee; ENSRNOG00000009867; Expressed in 10 organ(s), highest expression level in heart.
 Genevisible; Q07258; RN.
 GO; GO:0009986; C:cell surface; IDA:RGD.
 GO; GO:0062023; C:collagen-containing extracellular matrix; IEA:Ensembl.
 GO; GO:0005737; C:cytoplasm; IDA:RGD.
 GO; GO:0031012; C:extracellular matrix; ISS:AgBase.
 GO; GO:0005615; C:extracellular space; IDA:RGD.
 GO; GO:0043025; C:neuronal cell body; IDA:RGD.
 GO; GO:0005634; C:nucleus; IDA:RGD.
 GO; GO:0030141; C:secretory granule; IDA:RGD.
 GO; GO:0030315; C:T-tubule; IDA:RGD.
 GO; GO:0005125; F:cytokine activity; IBA:GO_Central.
 GO; GO:0008083; F:growth factor activity; IEA:UniProtKB-KW.
 GO; GO:0042802; F:identical protein binding; ISS:AgBase.
 GO; GO:0046982; F:protein heterodimerization activity; IDA:RGD.
 GO; GO:0050431; F:transforming growth factor beta binding; ISS:AgBase.
 GO; GO:0005160; F:transforming growth factor beta receptor binding; TAS:RGD.
 GO; GO:0034713; F:type I transforming growth factor beta receptor binding; ISS:AgBase.
 GO; GO:0005114; F:type II transforming growth factor beta receptor binding; ISS:AgBase.
 GO; GO:0034714; F:type III transforming growth factor beta receptor binding; ISS:AgBase.
 GO; GO:0000187; P:activation of MAPK activity; IDA:RGD.
 GO; GO:0007568; P:aging; IEP:RGD.
 GO; GO:0030509; P:BMP signaling pathway; IBA:GO_Central.
 GO; GO:0048468; P:cell development; IBA:GO_Central.
 GO; GO:0045216; P:cell-cell junction organization; ISS:AgBase.
 GO; GO:0070483; P:detection of hypoxia; ISS:AgBase.
 GO; GO:0048565; P:digestive tract development; IEP:RGD.
 GO; GO:0048702; P:embryonic neurocranium morphogenesis; IDA:RGD.
 GO; GO:0060325; P:face morphogenesis; ISS:AgBase.
 GO; GO:0007565; P:female pregnancy; IEP:RGD.
 GO; GO:0060364; P:frontal suture morphogenesis; IEP:RGD.
 GO; GO:0048839; P:inner ear development; IEP:RGD.
 GO; GO:0030324; P:lung development; NAS:RGD.
 GO; GO:0008285; P:negative regulation of cell proliferation; IDA:RGD.
 GO; GO:0010936; P:negative regulation of macrophage cytokine production; ISS:AgBase.
 GO; GO:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; IDA:RGD.
 GO; GO:1904706; P:negative regulation of vascular smooth muscle cell proliferation; IEA:Ensembl.
 GO; GO:0043932; P:ossification involved in bone remodeling; ISS:AgBase.
 GO; GO:0043065; P:positive regulation of apoptotic process; IDA:RGD.
 GO; GO:0030501; P:positive regulation of bone mineralization; ISS:AgBase.
 GO; GO:0051781; P:positive regulation of cell division; IEA:UniProtKB-KW.
 GO; GO:0008284; P:positive regulation of cell proliferation; ISS:BHF-UCL.
 GO; GO:0032967; P:positive regulation of collagen biosynthetic process; ISS:AgBase.
 GO; GO:0010718; P:positive regulation of epithelial to mesenchymal transition; ISS:AgBase.
 GO; GO:1905075; P:positive regulation of occluding junction disassembly; IEA:Ensembl.
 GO; GO:0010862; P:positive regulation of pathway-restricted SMAD protein phosphorylation; IBA:GO_Central.
 GO; GO:0050714; P:positive regulation of protein secretion; IEA:Ensembl.
 GO; GO:0051496; P:positive regulation of stress fiber assembly; IEA:Ensembl.
 GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:AgBase.
 GO; GO:0045601; P:regulation of endothelial cell differentiation; TAS:RGD.
 GO; GO:0030856; P:regulation of epithelial cell differentiation; TAS:RGD.
 GO; GO:0050678; P:regulation of epithelial cell proliferation; TAS:RGD.
 GO; GO:0043627; P:response to estrogen; IDA:RGD.
 GO; GO:0001666; P:response to hypoxia; IEP:RGD.
 GO; GO:0034616; P:response to laminar fluid shear stress; IEP:RGD.
 GO; GO:0032570; P:response to progesterone; ISS:AgBase.
 GO; GO:0007435; P:salivary gland morphogenesis; ISS:AgBase.
 GO; GO:0060395; P:SMAD protein signal transduction; IBA:GO_Central.
 GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; ISS:AgBase.
 GO; GO:0042060; P:wound healing; IEP:RGD.
 Gene3D; 2.10.90.10; -; 1.
 InterPro; IPR029034; Cystine-knot_cytokine.
 InterPro; IPR001839; TGF-b_C.
 InterPro; IPR001111; TGF-b_propeptide.
 InterPro; IPR016319; TGF-beta.
 InterPro; IPR015615; TGF-beta-rel.
 InterPro; IPR015618; TGFB3.
 InterPro; IPR017948; TGFb_CS.
 PANTHER; PTHR11848; PTHR11848; 1.
 Pfam; PF00019; TGF_beta; 1.
 Pfam; PF00688; TGFb_propeptide; 1.
 PIRSF; PIRSF001787; TGF-beta; 1.
 PRINTS; PR01423; TGFBETA.
 PRINTS; PR01426; TGFBETA3.
 SMART; SM00204; TGFB; 1.
 SUPFAM; SSF57501; SSF57501; 1.
 PROSITE; PS00250; TGF_BETA_1; 1.
 PROSITE; PS51362; TGF_BETA_2; 1.
 2: Evidence at transcript level;
 Cleavage on pair of basic residues; Complete proteome; Disulfide bond;
 Extracellular matrix; Glycoprotein; Growth factor; Methylation;
 Mitogen; Reference proteome; Secreted; Signal.
 SIGNAL        1     23       {ECO:0000255}.
 CHAIN        24    300       Latency-associated peptide.
                              {ECO:0000250|UniProtKB:P01137}.
                              /FTId=PRO_0000033802.
 CHAIN       301    412       Transforming growth factor beta-3.
                              {ECO:0000250|UniProtKB:P01137}.
                              /FTId=PRO_0000033803.
 MOTIF       261    263       Cell attachment site.
                              {ECO:0000250|UniProtKB:P01137}.
 MOD_RES     293    293       N5-methylglutamine.
                              {ECO:0000250|UniProtKB:P10600}.
 CARBOHYD     74     74       N-linked (GlcNAc...) asparagine.
                              {ECO:0000255}.
 CARBOHYD    135    135       N-linked (GlcNAc...) asparagine.
                              {ECO:0000255}.
 CARBOHYD    142    142       N-linked (GlcNAc...) asparagine.
                              {ECO:0000255}.
 DISULFID    307    316       {ECO:0000250|UniProtKB:P10600}.
 DISULFID    315    378       {ECO:0000250|UniProtKB:P10600}.
 DISULFID    344    409       {ECO:0000250|UniProtKB:P10600}.
 DISULFID    348    411       {ECO:0000250|UniProtKB:P10600}.
 DISULFID    377    377       Interchain.
                              {ECO:0000250|UniProtKB:P10600}.
 SEQUENCE   412 AA;  47116 MW;  24FD7D899090AA9D CRC64;
 MKMHLQRALV VLALLNLATV SLSLSTCTTL DFGHIKKKRV EAIRGQILSK LRLTSPPEPS
 VMTHVPYQVL ALYNSTRELL EEMHGEREEG CTQETSESEY YAKEIHKFDM IQGLAEHNEL
 AVCPKGITSK VFRFNVSSVE KNGTNLFRAE FRVLRVPNPS SKRTEQRIEL FQILRPDEHI
 AKQRYIGGKN LPTRGTAEWL SFDVTDTVRE WLLRRESNLG LEISIHCPCH TFQPNGDILE
 NVHEVMEIKF KGVDNEDDHG RGDLGRLKKQ KDHHNPHLIL MMIPPHRLDS PGQGGQRKKR
 ALDTNYCFRN LEENCCVRPL YIDFRQDLGW KWVHEPKGYY ANFCSGPCPY LRSSDTTHST
 VLGLYNTLNP EASASPCCVP QDLEPLTILY YVGRTPKVEQ LSNMVVKSCK CS

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